dehydroascorbic acid dimer | 27297-64-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: dehydroascorbic acid dimer
• 英文别名: dimer of L(+)-dehydroascorbic acid；DHA；(1R,3R,6R,7S,10R,12R,15R,16S)-3,7,12,16-tetrahydroxy-2,5,9,11,14,18-hexaoxapentacyclo[10.6.0.01,15.03,10.06,10]octadecane-4,13-dione
• CAS: 27297-64-9
• 化学式: C₁₂H₁₂O₁₂
• 分子量: 348.22
• InChiKey: DBAUAPYTRMIWBN-JZTKDPPESA-N

物化性质

• 沸点：
  831.2±65.0 °C(Predicted)
• 密度：
  2.20±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.3
• 重原子数：
  24
• 可旋转键数：
  0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  170
• 氢给体数：
  4
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  dehydroascorbic acid dimer 在 谷胱甘肽 、 recombinant Phanerochaete chrysosporium glutathione transferase Omega isoform 1 作用下， 生成 维生素 C
  参考文献：
  名称：

  Glutathione Transferases of Phanerochaete chrysosporium

  摘要：

  The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.

  DOI：

  10.1074/jbc.m110.194548
• 作为产物：
  描述：

  维生素 C 在 对苯醌 作用下， 生成 dehydroascorbic acid dimer
  参考文献：
  名称：

  Oxidation of ascorbic acid and dehydroascorbic acid by superoxide ion in aprotic media

  摘要：

  DOI：

  10.1021/ja00387a020

文献信息

• Preparation of dehydro-l-ascorbic acid dimer by air oxidation of l-ascorbic acid in the presence of catalytic amounts of copper(II) acetate and pyridine
  作者：Eleftheria K. Koliou、Panayiotis V. Ioannou

  DOI：10.1016/j.carres.2004.11.015

  日期：2005.2

  The catalytic system Cu(ACO)(2)-Pyridine 1:4 mol% in methanol, slowly catalyses the air oxidation of ascorbic acid to the 2-methyl hemi-ketal of dehydroascorbic acid 5, and hydrogen peroxide. However, with Cu(ACO)2-Pyridine 3:4 mol% the air oxidation is quite fast and no hydrogen peroxide is present at the end of the reaction. Removal of the catalyst and refluxing the foamy 5 in MeCN gives the oxidized, dimeric, dehydroascorbic acid in very good yields (similar to70%) contaminated by similar to1-2% MeCN. (C) 2004 Elsevier Ltd. All rights reserved.
• Oxidation of ascorbic acid and dehydroascorbic acid by superoxide ion in aprotic media
  作者：Donald T. Sawyer、Glaico Chiericato、Tohru Tsuchiya

  DOI：10.1021/ja00387a020

  日期：1982.11
• Glutathione Transferases of Phanerochaete chrysosporium
  作者：Edgar Meux、Pascalita Prosper、Andrew Ngadin、Claude Didierjean、Mélanie Morel、Stéphane Dumarçay、Tiphaine Lamant、Jean-Pierre Jacquot、Frédérique Favier、Eric Gelhaye

  DOI：10.1074/jbc.m110.194548

  日期：2011.3

  The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.